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Conserved domains on  [gi|545688449|ref|NP_001269982|]
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stathmin-4 isoform 2 [Homo sapiens]

Protein Classification

stathmin family protein( domain architecture ID 10467180)

stathmin family protein is a small regulatory phosphoprotein, similar to human stathmin that is involved in the regulation of the microtubule filament system by destabilizing microtubules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 76-198 5.19e-53

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


:

Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 166.37  E-value: 5.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688449   76 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 155
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 545688449  156 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKE 198
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEKE 124
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 76-198 5.19e-53

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 166.37  E-value: 5.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688449   76 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 155
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 545688449  156 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKE 198
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEKE 124
 
Name Accession Description Interval E-value
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 76-198 5.19e-53

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 166.37  E-value: 5.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688449   76 DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ 155
Cdd:pfam00836   2 DTEVKELEKRASGQAFEVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 545688449  156 KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKE 198
Cdd:pfam00836  82 KADEENNNFSKMAEEKLKQKMEAYKENREAQIAALKEKLKEKE 124
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 113-199 1.11e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.26  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688449  113 RRDPSLEEIQKKLEAAEERRKYQEAELlKHLAEKREHEREviqkaieennnfikMAkEKLAQKMESNKENREA---HLAA 189
Cdd:pfam10168 551 KHDLAREEIQKRVKLLKLQKEQQLQEL-QSLEEERKSLSE--------------RA-EKLAEKYEEIKDKQEKlmrRCKK 614

                          90
                  ....*....|
gi 545688449  190 MLERLQEKEP 199
Cdd:pfam10168 615 VLQRLNSQLP 624
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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